Curated Information
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Curated Information Page
PubMed Id: 16417524 
This page summarizes selected information from the article referenced above and curated into PhosphoSitePlus®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2012,40:D261-70). To learn more about the scope of PhosphoSitePlus®, click here.
Srinivas H, et al. (2006) Akt phosphorylates and suppresses the transactivation of retinoic acid receptor alpha. Biochem J 395, 653-62 16417524
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S96-p - RARA (human)
Orthologous residues
RARA (human): S96‑p, RARA (mouse): S96‑p, RARA (rat): S93‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site
 Relevant cell lines - cell types - tissues:  293T (epithelial), COS (fibroblast)
 Cellular systems studied:  cell lines
 Species studied:  monkey
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Akt1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE Akt1 (human) co-immunoprecipitation
Downstream Regulation
 Effect of modification (function):  activity, inhibited
 Effect of modification (process):  transcription, inhibited


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